p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity
about
High levels of Hsp90 cochaperone p23 promote tumor progression and poor prognosis in breast cancer by increasing lymph node metastases and drug resistanceThe 'active life' of Hsp90 complexesHsp90 is regulated by a switch point in the C-terminal domainMixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle.Differential modulation of functional dynamics and allosteric interactions in the Hsp90-cochaperone complexes with p23 and Aha1: a computational study.A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.Hsp-90 and the biology of nematodes.Detection of changes in gene regulatory patterns, elicited by perturbations of the Hsp90 molecular chaperone complex, by visualizing multiple experiments with an animation.Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function.Heat shock protein 90 as a drug target against protozoan infections: biochemical characterization of HSP90 from Plasmodium falciparum and Trypanosoma evansi and evaluation of its inhibitor as a candidate drug.A small heat shock protein is essential for thermotolerance and intracellular survival of Leishmania donovani.Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies.Post-translational modifications of Hsp90 and their contributions to chaperone regulationHsp90 molecular chaperone inhibitors: are we there yet?Leishmania donovani P23 protects parasites against HSP90 inhibitor-mediated growth arrest.The co-chaperone p23 promotes prostate cancer motility and metastasisBiology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Gedunin inactivates the co-chaperone p23 protein causing cancer cell death by apoptosis.Prolyl hydroxylase domain protein 2 (PHD2) binds a Pro-Xaa-Leu-Glu motif, linking it to the heat shock protein 90 pathwayHydrating for resistance to radicicol.Ailanthone targets p23 to overcome MDV3100 resistance in castration-resistant prostate cancer.Non-coding RNAs turn up the heat: an emerging layer of novel regulators in the mammalian heat shock responseContributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity.Co-chaperones of Hsp90 in Plasmodium falciparum and their concerted roles in cellular regulation.Hsp90 inhibition: elimination of shock and stress.HSP90AB1: Helping the good and the bad.Hsp90 inhibitors radicicol and geldanamycin have opposing effects on Leishmania Aha1-dependent proliferation.Mechanisms of Resistance to Hsp90 Inhibitor Drugs: A Complex Mosaic Emerges.HOP expression is regulated by p53 and RAS and characteristic of a cancer gene signature.Role of the HSP90-associated cochaperone p23 in enhancing activity of the androgen receptor and significance for prostate cancerDiscovery and biological activity of 6BrCaQ as an inhibitor of the Hsp90 protein folding machinery.Heat shock protein 90 localizes to the surface and augments virulence factors of Cryptococcus neoformans.The Mechanism of Hsp90 ATPase Stimulation by Aha1Methods to validate Hsp90 inhibitor specificity, to identify off-target effects, and to rethink approaches for further clinical development.Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones.
P2860
Q24623958-684D6F13-8496-4FFD-9F32-32B243FDA37FQ26829003-1104A272-4FC5-43E1-8273-D90718BE4216Q27933174-16F9E1BD-10E5-4BCE-AD57-5052F2D6EC75Q27935652-30699513-A579-4CDE-9B7F-59368B4B1AFFQ30353164-44472D90-92B3-4A51-9826-E1831DAFFDC3Q30402024-D57EEA8D-DC52-4D5B-A60A-58147BB6F451Q30491353-21F87CCF-1C23-4267-8F2A-ABFC6D56F7E5Q30501629-E32F6E8E-D8C5-4C03-9921-EC6B031A8182Q33669025-83D7646C-B7E4-43D4-A184-A95707C1DA6FQ34351999-2ACB9EAE-DA5F-4393-ABB0-E5B5EEBEDB58Q34433468-2481452C-271C-4BF0-9FFD-30E67EFA352BQ35313148-216E89B3-B1AB-429D-96E2-8A6AF6D5A032Q35581165-DC847422-8A08-4709-8F51-09369676F775Q35655105-1435C178-EEC7-4CDA-BFC5-76A56C7E721CQ35725137-24EC740F-6A85-4E39-9887-E38B2D04997DQ35876533-07A7FF3C-D115-4ECD-A78A-38C0424F8D6EQ36023274-BEC372CC-E68B-4FA4-ADBF-20B31E0E2515Q36666275-1371A8BC-7FFB-4012-8CF4-DB8F522612DFQ36742175-99F0495E-6E31-42ED-8727-3121B9C5C390Q37445819-ACCF0C93-234B-491C-B961-76104DAA98B1Q37508596-BD3D05FF-5684-455B-ABD2-FCA2F3D3605FQ37601131-ABAC5BCC-2E28-4FF0-85D1-AB7E883F10FDQ38111801-E38AE078-F123-40D2-B6F6-AFFEED7B3C53Q38190248-78D57854-5488-4298-BFDA-AD2AB8518514Q38291354-09A70840-5290-43A7-9D98-931B3BC5D39FQ38584468-A93A4454-E1A0-46E9-87DA-86D8C35171A8Q38895392-3BD247B9-88A2-4D14-8D6B-67282512AD10Q38976702-3E9471A8-0F21-4619-A36B-EBFC7BFB82E9Q39093264-FF022B37-1C4C-4513-BC47-48CCE9D250FDQ39296019-3DBB3C0F-090E-45A0-9857-D70BFB40FB8CQ39581399-2E67A882-6350-4321-A441-D855C53BDE36Q40103625-88C372AF-644B-4CDD-84F6-FF213F15CA4EQ41063812-0CF5F349-A623-40EA-B44A-A846B0091E3AQ48118580-C723661B-1615-4175-9CF8-3F70DCFA2E8EQ52651026-52B6AA85-E8D5-476C-B47A-3A60ADF68523
P2860
p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
p23/Sba1p protects against Hsp ...... s intrinsic chaperone activity
@ast
p23/Sba1p protects against Hsp ...... s intrinsic chaperone activity
@en
type
label
p23/Sba1p protects against Hsp ...... s intrinsic chaperone activity
@ast
p23/Sba1p protects against Hsp ...... s intrinsic chaperone activity
@en
prefLabel
p23/Sba1p protects against Hsp ...... s intrinsic chaperone activity
@ast
p23/Sba1p protects against Hsp ...... s intrinsic chaperone activity
@en
P2093
P2860
P356
P1476
p23/Sba1p protects against Hsp ...... s intrinsic chaperone activity
@en
P2093
Brian C Freeman
Didier Picard
Elena Suslova
Fedor Forafonov
Oyetunji A Toogun
P2860
P304
P356
10.1128/MCB.02246-07
P407
P50
P577
2008-03-24T00:00:00Z